| Literature DB >> 25479441 |
Raphael Eberle1, Norbert W Brattig2, Maria Trusch3, Hartmut Schlüter4, Mbunkah Daniel Achukwi5, Albert Eisenbarth6, Alfons Renz6, Eva Liebau7, Markus Perbandt8, Christian Betzel9.
Abstract
Parasitic helminths excrete or secrete a variety of functional molecules into the internal milieu of their mammalian hosts and arthropod vectors which reveal distinct immunomodulatory and other biological activities. We identified and initially characterized the low molecular weight peptide composition of the secretome from the filarial parasite Onchocerca ochengi. A total of 85 peptides were purified by liquid chromatography and further characterized by mass spectrometry. 72 of these peptides were derived from already described Onchocerca proteins and 13 peptide sequences are included in the sequence of uncharacterized proteins. Three peptides, similar to host defense peptides, revealed antibacterial activity. The present analysis confirms the putative involvement of low molecular weight compounds in the parasite-host cross-talk.Entities:
Keywords: Antibacterial activity; Excretory–secretory products; Filaria; Functional peptides; Onchocerca
Mesh:
Substances:
Year: 2014 PMID: 25479441 DOI: 10.1016/j.actatropica.2014.11.015
Source DB: PubMed Journal: Acta Trop ISSN: 0001-706X Impact factor: 3.112